Change search
ReferencesLink to record
Permanent link

Direct link
Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain
KTH, School of Biotechnology (BIO), Molecular Biotechnology.
KTH, School of Biotechnology (BIO), Molecular Biotechnology.
KTH, School of Biotechnology (BIO), Molecular Biotechnology.ORCID iD: 0000-0002-0695-5188
2011 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 17, no 6, 463-469 p.Article in journal (Refereed) Published
Abstract [en]

The Z-molecule is a small, engineered IgG-binding affinity protein derived from the immunoglobulin-binding domain B of Staphylococcus aureus protein A. The Z-domain consists of 58 amino acids forming a well-defined antiparallel three-helix structure. Two of the three helices are involved in ligand binding, whereas the third helix provides structural support to the three-helix bundle. The small size and the stable three-helix structure are two attractive properties comprised in the Z-domain, but a further reduction in size of the protein is valuable for several reasons. Reduction in size facilitates synthetic production of any protein-based molecule, which is beneficial from an economical viewpoint. In addition, a smaller protein is easier to manipulate through chemical modifications. By omitting the third stabilizing helix from the Z-domain and joining the N- and C-termini by a native peptide bond, the affinity protein obtains the advantageous properties of a smaller scaffold and in addition becomes resistant to exoproteases. We here demonstrate the synthesis and evaluation of a novel cyclic two-helix Z-domain. The molecule has retained affinity for its target protein, is resistant to heat treatment, and lacks both N- and C-termini. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.

Place, publisher, year, edition, pages
2011. Vol. 17, no 6, 463-469 p.
Keyword [en]
protein scaffold, Z-domain, two-helix protein, SPPS, IgG, affinity purification
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-34212DOI: 10.1002/psc.1346ISI: 000290633700007ScopusID: 2-s2.0-79955908750OAI: diva2:423486
QC 20110615Available from: 2011-06-15 Created: 2011-05-30 Last updated: 2011-06-15Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Järver, PeterMikaelsson, CeciliaKarlstrom Eriksson, Amelie
By organisation
Molecular Biotechnology
In the same journal
Journal of Peptide Science
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 28 hits
ReferencesLink to record
Permanent link

Direct link